位置:首页 > 蛋白库 > KTR1_YEAST
KTR1_YEAST
ID   KTR1_YEAST              Reviewed;         393 AA.
AC   P27810; D6W2G0;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=Alpha-1,2 mannosyltransferase KTR1;
DE            EC=2.4.1.-;
GN   Name=KTR1; OrderedLocusNames=YOR099W; ORFNames=YOR3189W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1541391; DOI=10.1093/genetics/130.2.273;
RA   Hill K., Boone C., Goebl M., Puccia R., Sdicu A.-M., Bussey H.;
RT   "Yeast KRE2 defines a new gene family encoding probable secretory proteins,
RT   and is required for the correct N-glycosylation of proteins.";
RL   Genetics 130:273-283(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9200815;
RX   DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA   Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA   Schwager C., Paces V., Sander C., Ansorge W.;
RT   "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL   Yeast 13:655-672(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=9020857; DOI=10.1042/bj3210289;
RA   Romero P.A., Lussier M., Sdicu A.-M., Bussey H.;
RT   "Ktr1p is an alpha-1,2-mannosyltransferase of Saccharomyces cerevisiae.
RT   Comparison of the enzymic properties of soluble recombinant Ktr1p and
RT   Kre2p/Mnt1p produced in Pichia pastoris.";
RL   Biochem. J. 321:289-295(1997).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX   PubMed=19756047; DOI=10.1038/msb.2009.64;
RA   Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT   "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT   new roles for protein glycosylation in eukaryotes.";
RL   Mol. Syst. Biol. 5:308-308(2009).
CC   -!- FUNCTION: Mannosyltransferase that transfers a mannose residue from
CC       GDP-mannose to a range of acceptors in vitro, forming an alpha-(1->2)-
CC       D-mannosyl-D-mannose linkage.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC       membrane protein.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC   -!- MISCELLANEOUS: Present with 5480 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 15 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X62941; CAA44713.1; -; Genomic_DNA.
DR   EMBL; X94335; CAA64021.1; -; Genomic_DNA.
DR   EMBL; Z75007; CAA99296.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10876.1; -; Genomic_DNA.
DR   PIR; S61659; S61659.
DR   RefSeq; NP_014742.1; NM_001183518.1.
DR   AlphaFoldDB; P27810; -.
DR   SMR; P27810; -.
DR   BioGRID; 34497; 122.
DR   DIP; DIP-7181N; -.
DR   IntAct; P27810; 1.
DR   MINT; P27810; -.
DR   STRING; 4932.YOR099W; -.
DR   CAZy; GT15; Glycosyltransferase Family 15.
DR   iPTMnet; P27810; -.
DR   MaxQB; P27810; -.
DR   PaxDb; P27810; -.
DR   PRIDE; P27810; -.
DR   EnsemblFungi; YOR099W_mRNA; YOR099W; YOR099W.
DR   GeneID; 854266; -.
DR   KEGG; sce:YOR099W; -.
DR   SGD; S000005625; KTR1.
DR   VEuPathDB; FungiDB:YOR099W; -.
DR   eggNOG; KOG4472; Eukaryota.
DR   GeneTree; ENSGT00940000176287; -.
DR   HOGENOM; CLU_024327_4_1_1; -.
DR   InParanoid; P27810; -.
DR   OMA; GYRHNPF; -.
DR   BioCyc; MetaCyc:G3O-33632-MON; -.
DR   BioCyc; YEAST:G3O-33632-MON; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:P27810; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P27810; protein.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IDA:SGD.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IBA:GO_Central.
DR   GO; GO:0097502; P:mannosylation; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IGI:SGD.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IGI:SGD.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002685; Glyco_trans_15.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR31121; PTHR31121; 1.
DR   Pfam; PF01793; Glyco_transf_15; 1.
DR   PIRSF; PIRSF018153; Glyco_trans_15; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..393
FT                   /note="Alpha-1,2 mannosyltransferase KTR1"
FT                   /id="PRO_0000208242"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..34
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..393
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          35..68
FT                   /note="Stem region"
FT                   /evidence="ECO:0000250"
FT   REGION          69..393
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        280
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   393 AA;  46022 MW;  F93DDF2953EA287B CRC64;
     MAKIMIPASK QPVYKKLGLL LVAVFTVYVF FHGAQYARGS APSPKYSTVL SSGSGYKYSK
     VELPKYTGPR EKATFVTLVR NRDLYSLAES IKSVEDRFNS KFNYDWVFLN DEEFTDEFKN
     VTSALVSGTT KYGVIPKEHW SFPEWIDEEK AAQVRKEMGE KRIIYGDSIS YRHMCRFESG
     FFYRHPLMDD YDWYWRVEPD IKLHCDIDYD VFKFMKDNKK KYAFAISIKE YEATIPTLWE
     TTRKFMEAHP ELIHENNMLD FVSDDQGLSY NLCHFWSNFE IAALDLWRSP AYSAYFDYLD
     REGGFFYERW GDAPVHSIGA ALFLDRSEIH HFGDIGYYHV PFHSCPIDTS IRLANKCDCD
     PSKDFTWHSY SCTTKFYNIN KLPKPAGWQN HIG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024